2gve

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{{STRUCTURE_2gve| PDB=2gve | SCENE= }}
{{STRUCTURE_2gve| PDB=2gve | SCENE= }}
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'''Time-of-Flight Neutron Diffraction Structure of D-Xylose Isomerase'''
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===Time-of-Flight Neutron Diffraction Structure of D-Xylose Isomerase===
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==Overview==
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Time-of-flight neutron diffraction has been used to locate hydrogen atoms that define the ionization states of amino acids in crystals of D-xylose isomerase. This enzyme, from Streptomyces rubiginosus, is one of the largest enzymes studied to date at high resolution (1.8 A) by this method. We have determined the position and orientation of a metal ion-bound water molecule that is located in the active site of the enzyme; this water has been thought to be involved in the isomerization step in which D-xylose is converted to D-xylulose or D-glucose to D-fructose. It is shown to be water (rather than a hydroxyl group) under the conditions of measurement (pH 8.0). Our analyses also reveal that one lysine probably has an -NH(2)-terminal group (rather than NH(3)(+)). The ionization state of each histidine residue also was determined. High-resolution x-ray studies (at 0.94 A) indicate disorder in some side chains when a truncated substrate is bound and suggest how some side chains might move during catalysis. This combination of time-of-flight neutron diffraction and x-ray diffraction can contribute greatly to the elucidation of enzyme mechanisms.
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(as it appears on PubMed at http://www.pubmed.gov), where 16707576 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16707576}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Locating active-site hydrogen atoms in D-xylose isomerase: time-of-flight neutron diffraction., Katz AK, Li X, Carrell HL, Hanson BL, Langan P, Coates L, Schoenborn BP, Glusker JP, Bunick GJ, Proc Natl Acad Sci U S A. 2006 May 30;103(22):8342-7. Epub 2006 May 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16707576 16707576]
Locating active-site hydrogen atoms in D-xylose isomerase: time-of-flight neutron diffraction., Katz AK, Li X, Carrell HL, Hanson BL, Langan P, Coates L, Schoenborn BP, Glusker JP, Bunick GJ, Proc Natl Acad Sci U S A. 2006 May 30;103(22):8342-7. Epub 2006 May 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16707576 16707576]
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Modes of binding substrates and their analogues to the enzyme D-xylose isomerase., Carrell HL, Hoier H, Glusker JP, Acta Crystallogr D Biol Crystallogr. 1994 Mar 1;50(Pt 2):113-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299449 15299449]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptomyces rubiginosus]]
[[Category: Streptomyces rubiginosus]]
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[[Category: Tim barrel-beta-alpha-barrel]]
[[Category: Tim barrel-beta-alpha-barrel]]
[[Category: Two metal binding site]]
[[Category: Two metal binding site]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:35:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:26:40 2008''

Revision as of 11:26, 29 July 2008

Image:2gve.png

Template:STRUCTURE 2gve

Time-of-Flight Neutron Diffraction Structure of D-Xylose Isomerase

Template:ABSTRACT PUBMED 16707576

About this Structure

2GVE is a Single protein structure of sequence from Streptomyces rubiginosus. Full crystallographic information is available from OCA.

Reference

Locating active-site hydrogen atoms in D-xylose isomerase: time-of-flight neutron diffraction., Katz AK, Li X, Carrell HL, Hanson BL, Langan P, Coates L, Schoenborn BP, Glusker JP, Bunick GJ, Proc Natl Acad Sci U S A. 2006 May 30;103(22):8342-7. Epub 2006 May 17. PMID:16707576

Modes of binding substrates and their analogues to the enzyme D-xylose isomerase., Carrell HL, Hoier H, Glusker JP, Acta Crystallogr D Biol Crystallogr. 1994 Mar 1;50(Pt 2):113-23. PMID:15299449

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